Specificity of an extracellular proteinase from Brevibacterium linens ATCC 9174 on bovine alpha(sub s1)-casein

Article Abstract:

The extracellular proteinase from Brevibacterium (B.) linens ATCC 9174, has no clear specificity for amino acids at positions P(sub 1) and P'(sub 1) in bovine alpha(sub s1)-casein. The proteinase however favours hydrophobic residues at the P(sub 2), P(sub 3), P(sub 4), P'(sub 2), P'(sub 3) and P'(sub 4) positions. The hydrolysis of casein by the proteinase is monitored using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The action of extracellular enzymes at the surface of casein produces low-molecular-mass peptides that diffuse into the cheese and confer it a characteristic flavor.

Observations, Gel electrophoresis

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Activity and purification of linenscin OC2, an antibacterial substance produced by Brevibacterium linens OC2, an orange cheese coryneform bacterium

Article Abstract:

Brevibacterium linens produce an antimicrobial compound called linenscin OC2 which kills gram-positive pathogenic bacteria such as Staphylococcus and Listeria but has no effect on gram-negative bacteria. Studies show that this compound is not affected much by temperature, proteolytic enzymes, organic solvents or pH. The molecular weight of linenscin OC2 has been estimated to be more than 285,000 and the molecular mass is less than 2,412 Da. Linenscin OC2 is not a bacteriocin and 90% of its amino acids are hydrophobic and are not electrically charged.

Antibacterial agents, Composition, Microbiological assay

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Specificity of an extracellular proteinase from Brevibacterium linens ATCC 9174 on bovine beta-casein

Article Abstract:

The specificity of the extracellular proteinase from Brevibacterium linens ATCC 9174 on bovine beta-casein was investigated. Hydrolysis was observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) and urea-PAGE. The major pH 4.6-soluble peptides were isolated and identified. The proteinase had a wide specificity for the amino acid residues found at the P1 and P'1 positions but indicated a preference for hydrophobic residues at the P2, P3, P4, P'2, P'3 and P'4 positions.

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